ID   CYSH_ERWCT              Reviewed;         244 AA.
AC   Q6D1A3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-NOV-2008, entry version 30.
DE   RecName: Full=Phosphoadenosine phosphosulfate reductase;
DE            EC=1.8.4.8;
DE   AltName: Full=PAPS reductase, thioredoxin dependent;
DE   AltName: Full=PAdoPS reductase;
DE   AltName: Full=3'-phosphoadenylylsulfate reductase;
DE   AltName: Full=PAPS sulfotransferase;
GN   Name=cysH; OrderedLocusNames=ECA3545;
OS   Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=29471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia
RT   carotovora subsp. atroseptica and characterization of virulence
RT   factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + sulfite +
CC       thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
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DR   EMBL; BX950851; CAG76443.1; -; Genomic_DNA.
DR   RefSeq; YP_051633.1; -.
DR   SMR; Q6D1A3; 2-230.
DR   GeneID; 2882116; -.
DR   GenomeReviews; BX950851_GR; ECA3545.
DR   KEGG; eca:ECA3545; -.
DR   NMPDR; fig|218491.3.peg.2191; -.
DR   HOGENOM; Q6D1A3; -.
DR   BioCyc; ECAR218491:ECA3545-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredo...; IEA:HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfa...; IEA:HAMAP.
DR   HAMAP; MF_00063; -; 1.
DR   InterPro; IPR004511; CysH.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR011800; PAPS_reductase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
DR   TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Oxidoreductase.
FT   CHAIN         1    244       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_1000008925.
SQ   SEQUENCE   244 AA;  27716 MW;  EB26CDD1D820378F CRC64;
     MAEFNLEALN ALPKDEQVAA LAAVNGQLEQ LSAQERVSWA LENLPGDFVL SSSFGIQAAI
     SLHLVTQQRP DIPVILTDTG YLFPETYQFI DALTEQLKLN LHVYRAAESP AWQESRYGKL
     WDQGVEGIER YNLLNKVEPM NRALSELNAG TWFAGLRREQ SGSRGELPVL AIQRGVFKFL
     PIIDWDNRTV YQYLKENGLS YHPLWDQGYL SVGDTHTTRK WEPGMSEEET RFFGLKRECG
     LHEG
//